Briggs John A G, Wilk Thomas, Fuller Stephen D
Division of Structural Biology, Wellcome Trust Centre for Human Genetics, Henry Wellcome Building for Genomic Medicine, University of Oxford, Roosevelt Drive, Headington, Oxford OX3 7BN, UK.
J Gen Virol. 2003 Apr;84(Pt 4):757-768. doi: 10.1099/vir.0.18779-0.
Co-infection of a host cell by two unrelated enveloped viruses can lead to the production of pseudotypes: virions containing the genome of one virus but the envelope proteins of both viruses. The selection of components during virus assembly must therefore be flexible enough to allow the incorporation of unrelated viral membrane proteins, yet specific enough to exclude the bulk of host proteins. This apparent contradiction has been termed the pseudotypic paradox. There is mounting evidence that lipid rafts play a role in the assembly pathway of non-icosahedral, enveloped viruses. Viral components are concentrated initially in localized regions of the plasma membrane via their interaction with lipid raft domains. Lateral interactions of viral structural proteins amplify the changes in local lipid composition which in turn enhance the concentration of viral proteins in the rafts. An affinity for lipid rafts may be the common feature of enveloped virus proteins that leads to the formation of pseudotypes.
病毒粒子含有一种病毒的基因组,但包膜蛋白来自两种病毒。因此,病毒组装过程中成分的选择必须足够灵活,以允许掺入不相关的病毒膜蛋白,但又要足够特异,以排除大部分宿主蛋白。这种明显的矛盾被称为假型悖论。越来越多的证据表明,脂筏在非二十面体包膜病毒的组装途径中发挥作用。病毒成分最初通过与脂筏结构域的相互作用而集中在质膜的局部区域。病毒结构蛋白的侧向相互作用放大了局部脂质组成的变化,这反过来又增强了病毒蛋白在脂筏中的浓度。对脂筏的亲和力可能是包膜病毒蛋白导致假型形成的共同特征。